ArticleMolecular and cellular biology1998
Interactions among Drosophila nuclear envelope proteins lamin, otefin, and YA.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 71 citations in OpenAlex.
- Review
- Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly inOpen biology · 2023Article
- Inner nuclear membrane protein TMEM201 promotes breast cancer metastasis by positive regulating TGFβ signaling.Oncogene · 2022Article
- Clock proteins regulate spatiotemporal organization of clock genes to control circadian rhythms.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Lamin is essential for nuclear localization of the GPI synthesis enzyme PIG-B and GPI-anchored protein production inJournal of cell science · 2020Article
- Laminopathies: what can humans learn from fruit flies.Cellular & molecular biology letters · 2018Review
- Non-farnesylated B-type lamin can tether chromatin inside the nucleus and its chromatin interaction requires the Ig-fold region.Chromosoma · 2017Article
- Functional analysis of centrosomal kinase substrates in Drosophila melanogaster reveals a new function of the nuclear envelope component otefin in cell cycle progression.Molecular and cellular biology · 2012Article
- Rab5 GTPase controls chromosome alignment through Lamin disassembly and relocation of the NuMA-like protein Mud to the poles during mitosis.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Lamin C and chromatin organization in Drosophila.Journal of genetics · 2010Article
- Lamin-binding Proteins.Cold Spring Harbor perspectives in biology · 2010Review
- Tissue-specific defects are caused by loss of the Drosophila MAN1 LEM domain protein.Genetics · 2008Article
- The LEM domain proteins emerin and LAP2alpha are dispensable for human immunodeficiency virus type 1 and murine leukemia virus infections.Journal of virology · 2008Article
- The two tempos of nuclear pore complex evolution: highly adapting proteins in an ancient frozen structure.Genome biology · 2005Article
- Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly.The Journal of cell biology · 2002Article
- The Drosophila nuclear lamina protein YA binds to DNA and histone H2B with four domains.Molecular biology of the cell · 2002Article
- A role for nuclear lamins in nuclear envelope assembly.The Journal of cell biology · 2001Article
- The Drosophila Su(var)2-10 locus regulates chromosome structure and function and encodes a member of the PIAS protein family.Genes & development · 2001Article
- LAP2 binds to BAF.DNA complexes: requirement for the LEM domain and modulation by variable regions.The EMBO journal · 2001Article
- The tail domain of lamin Dm0 binds histones H2A and H2B.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
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Authors and funding
10 authors at 6 institutions in 4 countries.
Funding
Abstract
The nuclear envelope plays many roles, including organizing nuclear structure and regulating nuclear events. Molecular associations of nuclear envelope proteins may contribute to the implementation of these functions. Lamin, otefin, and YA are the three Drosophila nuclear envelope proteins known in early embryos. We used the yeast two-hybrid system to explore the interactions between pairs of these proteins. The ubiquitous major lamina protein, lamin Dm, interacts with both otefin, a peripheral protein of the inner nuclear membrane, and YA, an essential, developmentally regulated protein of the nuclear lamina. In agreement with this interaction, lamin and otefin can be coimmunoprecipitated from the vesicle fraction of Drosophila embryos and colocalize in nuclear envelopes of Drosophila larval salivary gland nuclei. The two-hybrid system was further used to map the domains of interaction among lamin, otefin, and YA. Lamin's rod domain interacts with the complete otefin protein, with otefin's hydrophilic NH2-terminal domain, and with two different fragments derived from this domain. Analogous probing of the interaction between lamin and YA showed that the lamin rod and tail plus part of its head domain are needed for interaction with full-length YA in the two-hybrid system. YA's COOH-terminal region is necessary and sufficient for interaction with lamin. Our results suggest that interactions with lamin might mediate or stabilize the localization of otefin and YA in the nuclear lamina. They also suggest that the need for both otefin and lamin in mediating association of vesicles with chromatin might reflect the function of a protein complex that includes these two proteins.
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